IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
artículos
Título:
Structural characterization of alpha-synuclein in an aggregation prone state
Autor/es:
MIN-KYU CHO, GABRIELLE NODET, HAI-YOUNG KIM, MALENE R. JENSEN, PAU BERNADO, CLAUDIO O. FERNANDEZ, STEFAN BECKER, MARTIN BLACKLEDGE, MARKUS ZWECKSTETTER
Revista:
PROTEIN SCIENCE
Editorial:
JOHN WILEY & SONS INC
Referencias:
Año: 2009 vol. 18 p. 1840 - 1846
ISSN:
0961-8368
Resumen:
The relation of alpha-synuclein (aS) aggregation to Parkinson’s disease has long been recognized, but the pathogenic species and its molecular properties have yet to be identified. To obtain insight into the properties of aS in an aggregation-prone state, we studied the structural properties of aS at acidic pH using NMR spectroscopy and computation. NMR demonstrated that aS remains natively unfolded at lower pH, but secondary structure propensities were changed in proximity to acidic residues. The ensemble of conformations of aS at acidic pH is characterized by a rigidification and compaction of the Asp and Glu-rich C-terminal domain, an increased probability for proximity between the NAC-region and the C-terminal domain and a lower probability for interactions between the N- and C-terminal domains.